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Conserved domains on  [gi|7768709|dbj|BAA95504|]
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disintegrin-like and metalloprotease with thrombospondin type 1 motif, 5, partial [Homo sapiens]

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 10259619)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family| M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
269-412 6.62e-78

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


:

Pssm-ID: 239801  Cd Length: 207  Bit Score: 239.83  E-value: 6.62e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  269 VELLLVADASMARLY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273   3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7768709  348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEI 412
Cdd:cd04273  83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
66-178 6.68e-14

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 68.11  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709     66 QRRRSKGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDGSVGIAGFV-----PAGGGTSAPWRHRSHCFYRGTVDGSP 140
Cdd:pfam01562  13 RRRSLASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCYYQGHVEGHP 85
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 7768709    141 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEK 178
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
269-412 6.62e-78

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 239.83  E-value: 6.62e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  269 VELLLVADASMARLY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273   3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7768709  348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEI 412
Cdd:cd04273  83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
269-412 7.37e-16

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 75.80  E-value: 7.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709    269 VELLLVADASMARLYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLGDKDKsLEVSKNAATTLKNFCKWQ 345
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709    346 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEI 412
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHEL 139
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
66-178 6.68e-14

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 68.11  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709     66 QRRRSKGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDGSVGIAGFV-----PAGGGTSAPWRHRSHCFYRGTVDGSP 140
Cdd:pfam01562  13 RRRSLASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCYYQGHVEGHP 85
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 7768709    141 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEK 178
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
269-412 6.62e-78

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 239.83  E-value: 6.62e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  269 VELLLVADASMARLY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273   3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7768709  348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEI 412
Cdd:cd04273  83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
269-412 1.89e-23

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 96.72  E-value: 1.89e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  269 VELLLVADASMARLYGRG---LQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQ 345
Cdd:cd04267   3 IELVVVADHRMVSYFNSDeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7768709  346 HQHNQlgddheeHYDAAILFTREDLCGhhsCDTLGMADVGTICSPERSCAVIEDDG--LHAAFTVAHEI 412
Cdd:cd04267  83 AEGPI-------RHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHEL 141
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
269-412 1.22e-21

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 91.91  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  269 VELLLVADASMARLYGRGL---QHYLLTLASIANRLYSHAsienHIRLAVVKVVVLGDKDKsLEVSKNAATTLKNFCKWQ 345
Cdd:cd04269   3 VELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPL----NIRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLDWK 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  346 HqhNQLGDDHeeHYDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEI 412
Cdd:cd04269  78 R--SNLLPRK--PHDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSRNlllFAVTMAHEL 139
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
269-412 7.37e-16

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 75.80  E-value: 7.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709    269 VELLLVADASMARLYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLGDKDKsLEVSKNAATTLKNFCKWQ 345
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709    346 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEI 412
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHEL 139
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
66-178 6.68e-14

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 68.11  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709     66 QRRRSKGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDGSVGIAGFV-----PAGGGTSAPWRHRSHCFYRGTVDGSP 140
Cdd:pfam01562  13 RRRSLASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCYYQGHVEGHP 85
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 7768709    141 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEK 178
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
269-412 3.04e-06

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 47.73  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  269 VELLLVADASMARLYGRGLQ--HYLLTLASIANRLYShaSIEN-HIRLAVVKVVVlgDKDKSLEV--------SKNAATT 337
Cdd:cd04272   3 PELFVVVDYDHQSEFFSNEQliRYLAVMVNAANLRYR--DLKSpRIRLLLVGITI--SKDPDFEPyihpinygYIDAAET 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709  338 LKNFckwqhQHNQLGDDHEEHYDAAILFTREDLC----GHHSCDTLGMADVGTICSpERSCAVIED-----DGLHaafTV 408
Cdd:cd04272  79 LENF-----NEYVKKKRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDtpgsyYGVY---TM 149

                ....
gi 7768709  409 AHEI 412
Cdd:cd04272 150 THEL 153
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
268-412 2.45e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 44.72  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709    268 QVELLLVADASMARLYGR-GLQHYLLTLASIANRLYSHASienHIRLAVVKVVVLgDKDKSLEVSK----NAATTLKNFC 342
Cdd:pfam13688   4 TVALLVAADCSYVAAFGGdAAQANIINMVNTASNVYERDF---NISLGLVNLTIS-DSTCPYTPPAcstgDSSDRLSEFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7768709    343 ---KWQHQHNqlgddheehYDAAILFTredlcgHHSCDTLGMADVGTICSPERSCAVIEDDGLH--------AAFTVAHE 411
Cdd:pfam13688  80 dfsAWRGTQN---------DDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHE 144

                  .
gi 7768709    412 I 412
Cdd:pfam13688 145 I 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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